Abstract
Rap1A is a small G protein implicated in a spectrum of biological processes such as cell proliferation, adhesion, differentiation, and embryogenesis. The downstream effectors through which Rap1A mediates its diverse effects are largely unknown. Here we show that Rap1A, but not the related small G proteins Rap2 or Ras, binds the tumor suppressor Ras association domain family 1A (RASSF1A) in a manner that is regulated by phosphorylation of RASSF1A. Interaction with Rap1A is shown to influence the effect of RASSF1A on microtubule behavior.
Original language | English (US) |
---|---|
Pages (from-to) | 237-249 |
Number of pages | 13 |
Journal | Protein and Cell |
Volume | 2 |
Issue number | 3 |
DOIs | |
State | Published - 2011 |
Externally published | Yes |
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Keywords
- Microtubule
- Protein-protein interaction
- Rap1A
- RASSF1A
- Vimentin
ASJC Scopus subject areas
- Biotechnology
- Cell Biology
- Drug Discovery
- Biochemistry
Cite this
The tumor suppressor RASSF1A is a novel effector of small G protein Rap1A. / Verma, Sunil K.; Ganesan, Trivadi S.; Kishore, Uday; Parker, Peter J.
In: Protein and Cell, Vol. 2, No. 3, 2011, p. 237-249.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The tumor suppressor RASSF1A is a novel effector of small G protein Rap1A
AU - Verma, Sunil K.
AU - Ganesan, Trivadi S.
AU - Kishore, Uday
AU - Parker, Peter J.
PY - 2011
Y1 - 2011
N2 - Rap1A is a small G protein implicated in a spectrum of biological processes such as cell proliferation, adhesion, differentiation, and embryogenesis. The downstream effectors through which Rap1A mediates its diverse effects are largely unknown. Here we show that Rap1A, but not the related small G proteins Rap2 or Ras, binds the tumor suppressor Ras association domain family 1A (RASSF1A) in a manner that is regulated by phosphorylation of RASSF1A. Interaction with Rap1A is shown to influence the effect of RASSF1A on microtubule behavior.
AB - Rap1A is a small G protein implicated in a spectrum of biological processes such as cell proliferation, adhesion, differentiation, and embryogenesis. The downstream effectors through which Rap1A mediates its diverse effects are largely unknown. Here we show that Rap1A, but not the related small G proteins Rap2 or Ras, binds the tumor suppressor Ras association domain family 1A (RASSF1A) in a manner that is regulated by phosphorylation of RASSF1A. Interaction with Rap1A is shown to influence the effect of RASSF1A on microtubule behavior.
KW - Microtubule
KW - Protein-protein interaction
KW - Rap1A
KW - RASSF1A
KW - Vimentin
UR - http://www.scopus.com/inward/record.url?scp=79960049406&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79960049406&partnerID=8YFLogxK
U2 - 10.1007/s13238-011-1028-z
DO - 10.1007/s13238-011-1028-z
M3 - Article
C2 - 21468893
AN - SCOPUS:79960049406
VL - 2
SP - 237
EP - 249
JO - Protein and Cell
JF - Protein and Cell
SN - 1674-800X
IS - 3
ER -